[NMR paper] Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
J Am Chem Soc. 2017 Jun 14;
Authors: Good D, Pham C, Jagas J, Lewandowski JR, Ladizhansky V
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude...
nmrlearner
Journal club
0
06-15-2017 03:37 PM
[NMR paper] Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
J Phys Chem B. 2016 Dec 08;
Authors: Huang W, Emani PS, Varani G, Drobny GP
Abstract
Intrinsic motions may allow HIV-1 TAR RNA to change its conformation to form a functional complex with the Tat protein, which is essential for viral replication. Understanding the dynamic properties of TAR necessitates determining motion on the intermediate ns-?s time scale. To...
nmrlearner
Journal club
0
12-09-2016 06:09 PM
ConformationalDynamics of a Seven Transmembrane HelicalProtein Anabaena Sensory RhodopsinProbed by Solid-State NMR
ConformationalDynamics of a Seven Transmembrane HelicalProtein Anabaena Sensory RhodopsinProbed by Solid-State NMR
Daryl B. Good, Shenlin Wang, Meaghan E. Ward, Jochem Struppe, Leonid S. Brown, Jo?zef R. Lewandowski and Vladimir Ladizhansky
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja411633w/aop/images/medium/ja-2013-11633w_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja411633w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/MTq1JhQmGFU
nmrlearner
Journal club
0
02-05-2014 06:08 PM
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein.
Biophys J. 2011 Feb 2;100(3):711-9
Authors: Lu JX, Yau WM, Tycko R
The amyloid precursor protein (APP) is subject to proteolytic processing by ?-secretase within neuronal membranes, leading to Alzheimer's disease-associated ?-amyloid peptide production by cleavage near the midpoint of the*single...
nmrlearner
Journal club
0
02-02-2011 12:40 PM
[NMR paper] 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of
15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
Related Articles 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
J Magn Reson. 2005 Apr;173(2):322-7
Authors: Chekmenev EY, Hu J, Gor'kov PL, Brey WW, Cross TA, Ruuge A, Smirnov AI
This communication reports the first...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)
Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Related Articles Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Biophys J. 2000 Aug;79(2):767-75
Authors: Song Z, Kovacs FA, Wang J, Denny JK, Shekar SC, Quine JR, Cross TA
The M2 protein from the influenza A virus forms a proton channel in the virion that is essential for infection. This tetrameric protein...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...